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. 2004 Apr 26;101(19):7363–7368. doi: 10.1073/pnas.0401567101

Fig. 3.

Fig. 3.

Conservation of the γ-core motif among disulfide-containing antimicrobial peptides. The conserved γ-core motif (red) is indicated with corresponding sequences (GXC or CXG-C motifs are denoted in red text). Example molecules, peptide (source), are organized into four structural groups relative to the γ-core. γ Group: protegrin-1 (1PG1), gomesin (1KFP), tachyplesin-1 (1MA2), RTD-1 (1HVZ), thanatin (8TFV), and hepcidin (1M4F). γ-α Group: sapecin (1L4V), insect defensin A (1ICA), heliomycin (1I2U), drosomycin (1MYN), MGD-1 (1FJN), and charybdotoxin (2CRD). β-γ Group: HNP-3 (1DFN), RK-1 (1EWS), BNBD-12 (1BNB), HBD-1 (1E4S), HBD-2 (1E4Q), and mBD-8 (1E4R). β-γ-α Group: Ah-AMP-1 (1BK8), Rs-AFP-1 (1AYJ), Ps-Def-1 (1JKZ), γ-1-H-thionin (1GPT), γ-1-P-thionin (1GPS), and brazzein (1BRZ). Protegrin, gomesin, tachyplesin, RTD-1, and thanatin γ-core sequences (γ Group) are depicted in levomeric orientation. Other formatting is as in Fig. 2.